RR4_PSINU
ID RR4_PSINU Reviewed; 199 AA.
AC Q95CA6; Q8WI16;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=30S ribosomal protein S4, chloroplastic;
GN Name=rps4;
OS Psilotum nudum (Whisk fern) (Lycopodium nudum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Ophioglossidae; Psilotales; Psilotaceae; Psilotum.
OX NCBI_TaxID=3240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11214320; DOI=10.1038/35054555;
RA Pryer K.M., Schneider H., Smith A.R., Cranfill R., Wolf P.G., Hunt J.S.,
RA Sipes S.D.;
RT "Horsetails and ferns are a monophyletic group and the closest living
RT relatives to seed plants.";
RL Nature 409:618-622(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kingyoku;
RX PubMed=15240838; DOI=10.1093/molbev/msh203;
RA Nishiyama T., Wolf P.G., Kugita M., Sinclair R.B., Sugita M., Sugiura C.,
RA Wakasugi T., Yamada K., Yoshinaga K., Yamaguchi K., Ueda K., Hasebe M.;
RT "Chloroplast phylogeny indicates that bryophytes are monophyletic.";
RL Mol. Biol. Evol. 21:1813-1819(2004).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000250}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL26195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF313588; AAL26195.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP004638; BAB84218.1; -; Genomic_DNA.
DR RefSeq; NP_569631.1; NC_003386.1.
DR AlphaFoldDB; Q95CA6; -.
DR SMR; Q95CA6; -.
DR PRIDE; Q95CA6; -.
DR GeneID; 2545177; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..199
FT /note="30S ribosomal protein S4, chloroplastic"
FT /id="PRO_0000132658"
FT DOMAIN 84..146
FT /note="S4 RNA-binding"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 199 AA; 22911 MW; 8E99D1D93E16DF52 CRC64;
MESDQSKVES DQSKMESDQS KVESDQSISQ STSKKRSQYS LRLEAKQRLR FNYGVTERQL
LKYVCIAKKA RGSTGQVLLQ LLEMRLDNII FRLGLSPTIP GARQLVNHRH ILVNDQIVDI
PSYRCKPNDI ITVRDHQKSQ ELIKRNIKLA KIDEIPSHLN ISYLEETKPK GFINKIVDRG
SIGLEINELL VVEYYSRQA